Background: Recent studies have shown that human ferritin can be used as a reporter of gene expression for magnetic resonance imaging (MRI). Bacteria also encode three classes of ferritin-type molecules with iron accumulation properties.
Methods And Findings: Here, we investigated whether these bacterial ferritins can also be used as MRI reporter genes and which of the bacterial ferritins is the most suitable reporter. Bacterial ferritins were overexpressed in probiotic E. coli Nissle 1917. Cultures of these bacteria were analyzed and those generating highest MRI contrast were further investigated in tumor bearing mice. Among members of three classes of bacterial ferritin tested, bacterioferritin showed the most promise as a reporter gene. Although all three proteins accumulated similar amounts of iron when overexpressed individually, bacterioferritin showed the highest contrast change. By site-directed mutagenesis we also show that the heme iron, a unique part of the bacterioferritin molecule, is not critical for MRI contrast change. Tumor-specific induction of bacterioferritin-expression in colonized tumors resulted in contrast changes within the bacteria-colonized tumors.
Conclusions: Our data suggest that colonization and gene expression by live vectors expressing bacterioferritin can be monitored by MRI due to contrast changes.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3184983 | PMC |
| http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0025409 | PLOS |
Publication Analysis
Top Keywords
Similar Publications
Impact of p. Gingivalis-induced chronic apical periodontitis on systemic iron homeostasis via the hepatic IL-6/STAT3/Hepcidin signaling pathway.
Int Immunopharmacol
January 2025
State Key Laboratory of Oral Diseases & National Center of Stomatology & National Clinical Research Center for Oral Diseases & Department of Operative Dentistry and Endodontics West China Hospital of Stomatology, Sichuan University, Chengdu 610041, China. Electronic address:
Background And Aims: Chronic apical periodontitis (CAP), an inflammatory disease of the oral cavity caused by bacterial infections with Porphyromonas gingivalis (P. gingivalis) as a key pathogen, has been associated with systemic effects, potentially influencing distant organs including liver. The liver plays a key role in iron metabolism and immunity by hepcidin.
View Article and Find Full Text PDFA Closer Look at the FeS Heme Bonds in Azotobacter vinelandii Bacterioferritin: QM/MM and Local Mode Analysis.
J Comput Chem
January 2025
Chemistry Department, Southern Methodist University, Dallas, Texas, USA.
Using the QM/MM methodology and a local mode analysis, we investigated a character and a strength of FeS bonds of heme groups in oxidized and reduced forms of Bacterioferritin from Azotobacter vinelandii. The strength of the FeS bonds was correlated with a bond length, an energy density at a bond critical point, and a charge difference of the F and S atoms. Changing the oxidation state from ferrous to ferric generally makes the FeS bonds weaker, longer, more covalent, and more polar.
View Article and Find Full Text PDFFerritin-based hybrid macromolecules experience unusual shift of stoichiometry distribution.
Int J Biol Macromol
December 2024
Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, 141700 Dolgoprudny, Russian Federation; Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, 141980, Russian Federation. Electronic address:
Article Synopsis
- Ferritin-based hybrids are large macromolecules with potential uses in drug delivery and vaccines, but their design is complicated.
- Researchers designed hybrids using ferritin from Helicobacter pylori and a Small Ubiquitin-like Modifier, discovering that their assembly was influenced by varying preparation methods.
- They developed a quantitative model to analyze how different stoichiometries affected the structure of these hybrids, revealing unexpected patterns and establishing a framework for better design of ferritin-based systems.
Physicochemical features of subunit interfaces and their role in self-assembly across the ferritin superfamily.
Structure
December 2024
Department of Bioscience and Bioengineering, Indian Institute of Technology Jodhpur, NH 62, Nagaur Road, Karwar 342030, Jodhpur, Rajasthan, India. Electronic address:
Ferritins are ubiquitous and play a critical role in iron homeostasis. They are classified into four main subfamilies: classical, bacterial, bacterioferritin, and Dps. These are characterized by subunits with a four-helical bundle domain and interact through three distinct regions-one antiparallel interface (IntA) and two perpendicular interfaces (IntB and IntC), collectively forming a cage-like structure.
View Article and Find Full Text PDFProlonged self-assembly of H. pylori ferritin globules at physiological conditions.
Biochem Biophys Res Commun
January 2025
Research Center for Molecular Mechanisms of Aging and Age-Related Diseases, Moscow Institute of Physics and Technology, Dolgoprudny, 141700, Russian Federation; Frank Laboratory of Neutron Physics, Joint Institute for Nuclear Research, Dubna, 141980, Russian Federation. Electronic address:
One of the promising drug delivery tools is ferritin, which features high stability at a wide range of conditions and protects cargo by its spherical protein shell. We studied the self-assembly into homoglobules of ferritin from H. pylori and a chimeric protein ferritin-SUMO.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!